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PBPB_ECOLI
ID   PBPB_ECOLI              Reviewed;         844 AA.
AC   P02919; P75664;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   03-AUG-2022, entry version 218.
DE   RecName: Full=Penicillin-binding protein 1B;
DE            Short=PBP-1b;
DE            Short=PBP1b;
DE   AltName: Full=Murein polymerase;
DE   Includes:
DE     RecName: Full=Penicillin-insensitive transglycosylase;
DE              EC=2.4.1.129 {ECO:0000269|PubMed:19458048, ECO:0000269|PubMed:6389538};
DE     AltName: Full=Peptidoglycan TGase;
DE     AltName: Full=Peptidoglycan glycosyltransferase;
DE   Includes:
DE     RecName: Full=Penicillin-sensitive transpeptidase;
DE              EC=3.4.16.4 {ECO:0000269|PubMed:6389538};
DE     AltName: Full=DD-transpeptidase;
GN   Name=mrcB; Synonyms=pbpF, ponB; OrderedLocusNames=b0149, JW0145;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3882429; DOI=10.1111/j.1432-1033.1985.tb08768.x;
RA   Broome-Smith J.K., Edelman A., Yousif S., Spratt B.G.;
RT   "The nucleotide sequences of the ponA and ponB genes encoding penicillin-
RT   binding protein 1A and 1B of Escherichia coli K12.";
RL   Eur. J. Biochem. 147:437-446(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA   Fujita N., Mori H., Yura T., Ishihama A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT   4.1 min (110,917-193,643 bp) region.";
RL   Nucleic Acids Res. 22:1637-1639(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 103
RP   AND 754.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 497-525.
RC   STRAIN=K12;
RX   PubMed=3920658; DOI=10.1073/pnas.82.7.1999;
RA   Keck W., Glauner B., Schwarz U., Broome-Smith J.K., Spratt B.G.;
RT   "Sequences of the active-site peptides of three of the high-Mr penicillin-
RT   binding proteins of Escherichia coli K-12.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:1999-2003(1985).
RN   [6]
RP   CATALYTIC ACTIVITY.
RX   PubMed=6389538; DOI=10.1016/s0021-9258(18)89835-0;
RA   Nakagawa J., Tamaki S., Tomioka S., Matsuhashi M.;
RT   "Functional biosynthesis of cell wall peptidoglycan by polymorphic
RT   bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia
RT   coli with activities of transglycosylase and transpeptidase.";
RL   J. Biol. Chem. 259:13937-13946(1984).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=8645198; DOI=10.1042/bj3160149;
RA   Wang C.C., Schultz D.R., Nicholas R.A.;
RT   "Localization of a putative second membrane association site in penicillin-
RT   binding protein 1B of Escherichia coli.";
RL   Biochem. J. 316:149-156(1996).
RN   [8]
RP   TOPOLOGY.
RX   PubMed=9244263; DOI=10.1128/jb.179.15.4761-4767.1997;
RA   Lefevre F., Remy M.-H., Masson J.-M.;
RT   "Topographical and functional investigation of Escherichia coli penicillin-
RT   binding protein 1b by alanine stretch scanning mutagenesis.";
RL   J. Bacteriol. 179:4761-4767(1997).
RN   [9]
RP   TOPOLOGY.
RX   PubMed=3330753; DOI=10.1111/j.1365-2958.1987.tb00533.x;
RA   Edelman A., Bowler L., Broome-Smith J.K., Spratt B.G.;
RT   "Use of a beta-lactamase fusion vector to investigate the organization of
RT   penicillin-binding protein 1B in the cytoplasmic membrane of Escherichia
RT   coli.";
RL   Mol. Microbiol. 1:101-106(1987).
RN   [10]
RP   DIMERIZATION.
RX   PubMed=1885547; DOI=10.1128/jb.173.18.5740-5746.1991;
RA   Zijderveld C.A., Aarsman M.E., den Blaauwen T., Nanninga N.;
RT   "Penicillin-binding protein 1B of Escherichia coli exists in dimeric
RT   forms.";
RL   J. Bacteriol. 173:5740-5746(1991).
RN   [11]
RP   INTERACTION WITH MIPA AND MLTA.
RC   STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX   PubMed=10037771; DOI=10.1074/jbc.274.10.6726;
RA   Vollmer W., von Rechenberg M., Hoeltje J.-V.;
RT   "Demonstration of molecular interactions between the murein polymerase
RT   PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of
RT   Escherichia coli.";
RL   J. Biol. Chem. 274:6726-6734(1999).
RN   [12]
RP   ACTIVE SITE SER-510, AND MUTAGENESIS OF GLU-233; ASP-234 AND GLU-290.
RC   STRAIN=EJ801;
RX   PubMed=10564478; DOI=10.1046/j.1365-2958.1999.01612.x;
RA   Terrak M., Ghosh T.K., van Heijenoort J., Van Beeumen J., Lampilas M.,
RA   Aszodi J., Ayala J.A., Ghuysen J.-M., Nguyen-Disteche M.;
RT   "The catalytic, glycosyl transferase and acyl transferase modules of the
RT   cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of
RT   Escherichia coli.";
RL   Mol. Microbiol. 34:350-364(1999).
RN   [13]
RP   REVIEW.
RX   PubMed=9841666; DOI=10.1128/mmbr.62.4.1079-1093.1998;
RA   Goffin C., Ghuysen J.-M.;
RT   "Multimodular penicillin-binding proteins: an enigmatic family of orthologs
RT   and paralogs.";
RL   Microbiol. Mol. Biol. Rev. 62:1079-1093(1998).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 58-804 IN COMPLEX WITH
RP   MOENOMYCIN, PARTIAL PROTEIN SEQUENCE, INTERACTION WITH MLTA; UVRA; FTSL AND
RP   FTSN, MEMBRANE TOPOLOGY, CATALYTIC ACTIVITY, DOMAIN, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=19458048; DOI=10.1073/pnas.0904030106;
RA   Sung M.-T., Lai Y.-T., Huang C.-Y., Chou L.-Y., Shih H.-W., Cheng W.-C.,
RA   Wong C.-H., Ma C.;
RT   "Crystal structure of the membrane-bound bifunctional transglycosylase
RT   PBP1b from Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8824-8829(2009).
CC   -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC       from the lipid intermediates. The enzyme has a penicillin-insensitive
CC       transglycosylase N-terminal domain (formation of linear glycan strands)
CC       and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC       linking of the peptide subunits).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000269|PubMed:19458048, ECO:0000269|PubMed:6389538};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000269|PubMed:6389538};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBUNIT: Forms a trimeric complex with MipA and MltA. Has also been
CC       shown to exist as monomer or homodimer; homodimer of Alpha and Gamma
CC       isozymes can be found. Interacts with UvrA, FtsL and FtsN.
CC       {ECO:0000269|PubMed:10037771, ECO:0000269|PubMed:19458048}.
CC   -!- INTERACTION:
CC       P02919; P0AD68: ftsI; NbExp=3; IntAct=EBI-909769, EBI-548564;
CC       P02919; P29131: ftsN; NbExp=7; IntAct=EBI-909769, EBI-1134233;
CC       P02919; P0AB38: lpoB; NbExp=4; IntAct=EBI-909769, EBI-3405489;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Alpha; Synonyms=Long;
CC         IsoId=P02919-1; Sequence=Displayed;
CC       Name=Gamma; Synonyms=Short;
CC         IsoId=P02919-2; Sequence=VSP_018737;
CC   -!- DOMAIN: The UvrB domain 2 homolog region (UB2H domain) is important for
CC       interaction with MltA. {ECO:0000269|PubMed:19458048}.
CC   -!- MISCELLANEOUS: A third isozyme, Beta, lacking the first 25 N-terminal
CC       amino acids of the isoform Alpha and a fourth isozyme, Delta, have been
CC       found, but seem to result from the artifactual degradation of the
CC       isoform Alpha and isoform Gamma respectively.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA26099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X02163; CAA26098.1; -; Genomic_DNA.
DR   EMBL; X02163; CAA26099.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73260.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAB96725.2; -; Genomic_DNA.
DR   PIR; E64738; ZPECPB.
DR   RefSeq; NP_414691.1; NC_000913.3.
DR   RefSeq; WP_000918162.1; NZ_STEB01000032.1.
DR   PDB; 3FWL; X-ray; 3.09 A; A=58-804.
DR   PDB; 3VMA; X-ray; 2.16 A; A=58-804.
DR   PDB; 5FGZ; X-ray; 2.85 A; A=58-804.
DR   PDB; 5HL9; X-ray; 2.70 A; A=58-804.
DR   PDB; 5HLA; X-ray; 2.36 A; A=58-804.
DR   PDB; 5HLB; X-ray; 2.42 A; A=58-804.
DR   PDB; 5HLD; X-ray; 2.31 A; A=58-804.
DR   PDB; 6FZK; NMR; -; A=108-200.
DR   PDB; 6G5R; NMR; -; A=108-200.
DR   PDB; 6YN0; X-ray; 2.40 A; A=58-804.
DR   PDB; 7LQ6; EM; 3.28 A; A=58-804.
DR   PDBsum; 3FWL; -.
DR   PDBsum; 3VMA; -.
DR   PDBsum; 5FGZ; -.
DR   PDBsum; 5HL9; -.
DR   PDBsum; 5HLA; -.
DR   PDBsum; 5HLB; -.
DR   PDBsum; 5HLD; -.
DR   PDBsum; 6FZK; -.
DR   PDBsum; 6G5R; -.
DR   PDBsum; 6YN0; -.
DR   PDBsum; 7LQ6; -.
DR   AlphaFoldDB; P02919; -.
DR   SMR; P02919; -.
DR   BioGRID; 4260880; 259.
DR   DIP; DIP-10252N; -.
DR   IntAct; P02919; 15.
DR   STRING; 511145.b0149; -.
DR   BindingDB; P02919; -.
DR   ChEMBL; CHEMBL1814; -.
DR   DrugBank; DB01602; Bacampicillin.
DR   DrugBank; DB00578; Carbenicillin.
DR   DrugBank; DB09319; Carindacillin.
DR   DrugBank; DB01414; Cefacetrile.
DR   DrugBank; DB01327; Cefazolin.
DR   DrugBank; DB00274; Cefmetazole.
DR   DrugBank; DB01328; Cefonicid.
DR   DrugBank; DB01329; Cefoperazone.
DR   DrugBank; DB01331; Cefoxitin.
DR   DrugBank; DB00430; Cefpiramide.
DR   DrugBank; DB11367; Cefroxadine.
DR   DrugBank; DB00438; Ceftazidime.
DR   DrugBank; DB01415; Ceftibuten.
DR   DrugBank; DB01332; Ceftizoxime.
DR   DrugBank; DB09050; Ceftolozane.
DR   DrugBank; DB00689; Cephaloglycin.
DR   DrugBank; DB01000; Cyclacillin.
DR   DrugBank; DB06211; Doripenem.
DR   DrugBank; DB00303; Ertapenem.
DR   DrugBank; DB01598; Imipenem.
DR   DrugBank; DB04570; Latamoxef.
DR   DrugCentral; P02919; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   jPOST; P02919; -.
DR   PaxDb; P02919; -.
DR   PRIDE; P02919; -.
DR   EnsemblBacteria; AAC73260; AAC73260; b0149.
DR   EnsemblBacteria; BAB96725; BAB96725; BAB96725.
DR   GeneID; 944843; -.
DR   KEGG; ecj:JW0145; -.
DR   KEGG; eco:b0149; -.
DR   PATRIC; fig|1411691.4.peg.2132; -.
DR   EchoBASE; EB0600; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_2_7_6; -.
DR   InParanoid; P02919; -.
DR   OMA; VHGMGLA; -.
DR   PhylomeDB; P02919; -.
DR   BioCyc; EcoCyc:EG10605-MON; -.
DR   BioCyc; MetaCyc:EG10605-MON; -.
DR   BRENDA; 2.4.1.129; 2026.
DR   UniPathway; UPA00219; -.
DR   EvolutionaryTrace; P02919; -.
DR   PRO; PR:P02919; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
DR   GO; GO:0008658; F:penicillin binding; IDA:EcoCyc.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IDA:EcoCyc.
DR   GO; GO:0071433; P:cell wall repair; IDA:EcoCyc.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:EcoCyc.
DR   GO; GO:0051518; P:positive regulation of bipolar cell growth; IDA:EcoliWiki.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR   GO; GO:0010165; P:response to X-ray; IMP:EcoCyc.
DR   Gene3D; 1.10.3810.10; -; 1.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR032730; PBP1b_TM.
DR   InterPro; IPR011813; PBP_1b.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR028166; UB2H.
DR   Pfam; PF14812; PBP1_TM; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   Pfam; PF14814; UB2H; 1.
DR   PIRSF; PIRSF002799; PBP_1b; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR02071; PBP_1b; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative initiation; Antibiotic resistance;
KW   Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
KW   Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Glycosyltransferase; Hydrolase; Membrane; Multifunctional enzyme;
KW   Peptidoglycan synthesis; Protease; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..844
FT                   /note="Penicillin-binding protein 1B"
FT                   /id="PRO_0000012145"
FT   TOPO_DOM        1..63
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        64..87
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        88..844
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..250
FT                   /note="Membrane association"
FT   REGION          109..200
FT                   /note="UvrB domain 2 homolog"
FT   REGION          195..367
FT                   /note="Transglycosylase"
FT   REGION          444..736
FT                   /note="Transpeptidase"
FT   REGION          793..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..828
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        233
FT                   /note="Proton donor; for transglycosylase activity"
FT                   /evidence="ECO:0000305|PubMed:10564478"
FT   ACT_SITE        510
FT                   /note="Acyl-ester intermediate; for transpeptidase
FT                   activity"
FT                   /evidence="ECO:0000269|PubMed:10564478"
FT   VAR_SEQ         1..45
FT                   /note="Missing (in isoform Gamma)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018737"
FT   MUTAGEN         233
FT                   /note="E->Q: Loss of wild-type glycan chain elongation
FT                   activity. No complementation in strain defective in PBP-
FT                   1b."
FT                   /evidence="ECO:0000269|PubMed:10564478"
FT   MUTAGEN         234
FT                   /note="D->N: 7-fold decrease in catalytic activity. No
FT                   complementation in strain defective in PBP-1b."
FT                   /evidence="ECO:0000269|PubMed:10564478"
FT   MUTAGEN         290
FT                   /note="E->Q: 11-fold decrease in catalytic activity. Shows
FT                   complementation activity in strain defective in PBP-1b."
FT                   /evidence="ECO:0000269|PubMed:10564478"
FT   CONFLICT        103
FT                   /note="P -> A (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        754
FT                   /note="P -> PTP (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   TURN            69..72
FT                   /evidence="ECO:0007829|PDB:3FWL"
FT   HELIX           76..88
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           90..93
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          104..107
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:5HL9"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:6FZK"
FT   HELIX           121..130
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          144..148
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          151..156
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          169..176
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          179..185
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   TURN            186..189
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          193..196
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          201..205
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          210..212
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           218..220
FT                   /evidence="ECO:0007829|PDB:5HLD"
FT   HELIX           223..231
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          234..236
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:3FWL"
FT   HELIX           241..243
FT                   /evidence="ECO:0007829|PDB:3FWL"
FT   TURN            247..249
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           268..276
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          280..282
FT                   /evidence="ECO:0007829|PDB:5FGZ"
FT   HELIX           284..300
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           303..310
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   TURN            311..313
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          314..319
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          322..326
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           327..335
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           339..341
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           344..355
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          356..360
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   TURN            362..364
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           366..382
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          383..385
FT                   /evidence="ECO:0007829|PDB:5HLB"
FT   HELIX           388..395
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          408..411
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           412..426
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   TURN            430..432
FT                   /evidence="ECO:0007829|PDB:5HLD"
FT   STRAND          433..435
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          437..440
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           444..464
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          471..478
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   TURN            479..481
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          483..488
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          490..492
FT                   /evidence="ECO:0007829|PDB:5HL9"
FT   STRAND          493..495
FT                   /evidence="ECO:0007829|PDB:5HLD"
FT   HELIX           500..503
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           509..512
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           513..521
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   TURN            524..526
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          532..534
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          540..542
FT                   /evidence="ECO:0007829|PDB:5HL9"
FT   STRAND          543..545
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          546..548
FT                   /evidence="ECO:0007829|PDB:5HL9"
FT   STRAND          561..564
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           565..570
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           574..584
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           586..596
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           600..602
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           607..611
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           618..629
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          632..634
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          640..644
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          646..648
FT                   /evidence="ECO:0007829|PDB:3FWL"
FT   STRAND          650..653
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           664..679
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           684..689
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           691..693
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          696..701
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           703..705
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          706..713
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          715..724
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           737..749
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          763..768
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          774..777
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   STRAND          780..786
FT                   /evidence="ECO:0007829|PDB:3VMA"
FT   HELIX           792..797
FT                   /evidence="ECO:0007829|PDB:3VMA"
SQ   SEQUENCE   844 AA;  94293 MW;  CED0A19FAC73961E CRC64;
     MAGNDREPIG RKGKPTRPVK QKVSRRRYED DDDYDDYDDY EDEEPMPRKG KGKGKGRKPR
     GKRGWLWLLL KLAIVFAVLI AIYGVYLDQK IRSRIDGKVW QLPAAVYGRM VNLEPDMTIS
     KNEMVKLLEA TQYRQVSKMT RPGEFTVQAN SIEMIRRPFD FPDSKEGQVR ARLTFDGDHL
     ATIVNMENNR QFGFFRLDPR LITMISSPNG EQRLFVPRSG FPDLLVDTLL ATEDRHFYEH
     DGISLYSIGR AVLANLTAGR TVQGASTLTQ QLVKNLFLSS ERSYWRKANE AYMALIMDAR
     YSKDRILELY MNEVYLGQSG DNEIRGFPLA SLYYFGRPVE ELSLDQQALL VGMVKGASIY
     NPWRNPKLAL ERRNLVLRLL QQQQIIDQEL YDMLSARPLG VQPRGGVISP QPAFMQLVRQ
     ELQAKLGDKV KDLSGVKIFT TFDSVAQDAA EKAAVEGIPA LKKQRKLSDL ETAIVVVDRF
     SGEVRAMVGG SEPQFAGYNR AMQARRSIGS LAKPATYLTA LSQPKIYRLN TWIADAPIAL
     RQPNGQVWSP QNDDRRYSES GRVMLVDALT RSMNVPTVNL GMALGLPAVT ETWIKLGVPK
     DQLHPVPAML LGALNLTPIE VAQAFQTIAS GGNRAPLSAL RSVIAEDGKV LYQSFPQAER
     AVPAQAAYLT LWTMQQVVQR GTGRQLGAKY PNLHLAGKTG TTNNNVDTWF AGIDGSTVTI
     TWVGRDNNQP TKLYGASGAM SIYQRYLANQ TPTPLNLVPP EDIADMGVDY DGNFVCSGGM
     RILPVWTSDP QSLCQQSEMQ QQPSGNPFDQ SSQPQQQPQQ QPAQQEQKDS DGVAGWIKDM
     FGSN
 
 
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